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H6512

Sigma-Aldrich

Heparinase II from Flavobacterium heparinum

Lyophilized powder stabilized with approx. 25% bovine serum albumin, lyophilized powder, ≥100 units/mg protein (enzyme + BSA)

Sinônimo(s):

Heparin lyase II

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About This Item

Número CAS:
149371-12-0
Número MDL:
MFCD00131319
Código UNSPSC:
12352204
NACRES:
NA.54

fonte biológica

bacterial (Flavobacterium heparinum)

Nível de qualidade

200

conjugado

conjugate (Glucosaminoglycan)

Formulário

lyophilized powder

atividade específica

≥100 units/mg protein (enzyme + BSA)

peso molecular

84.1 kDa

temperatura de armazenamento

−20°C

Descrição geral

Heparinase II is one of three key heparin-degrading enzymes of Flavobacterium heparinum (also known as Pedobacter heparinus1). It belongs to the polysaccharide lyases family PL21.

Aplicação

Heparinase II from Flavobacterium heparinum has been used:
  • for digestion of heparin sulfate during exosome isolation
  • for digestion of heparin sulfate in notochordal cell conditioned media (NCCM) to investigate the content of glycosaminoglycans in NCCM
  • as a component of digestion buffer during cell surface glycan processing
  • as a component of heparin lyase (HSase) mix to remove the heparin sulfate on the 293ͰT/ACE2 cell surface and study the effect of histones on the infectivity of pseudovirus

Ações bioquímicas/fisiológicas

Heparinase II cleaves heparan sulfate, and to a lesser extent heparin (relative activity about 2:1), at the α (1-4) linkages between hexosamines and uronic acid residues (both glucuronic and iduronic), yielding mainly disaccharides. Heparinase II has the broadest substrate specificity of the three heparinases Heparinase enzymes helps in decoding the complex structures of substrates. Heparin interferes with DNA transcription in PCR and in reverse transcription of RNA. Heparinase II has been used to remove heparin for downstream analysis of genomic DNA.

Definição da unidade

One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.0 at 25 °C. One International Unit (I.U.) is equivalent to approx. 600 Sigma units.

Outras notas

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

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Certificados de análise (COA)

Lot/Batch Number
SLCJ0337
SLCJ0338
SLCD0812
SLBZ1235
SLBZ1237

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Moffat, C.F., et al.
Proc. 8th Int. Symp. Glycoconjugates, 1, 79-79 (1985)
Judith Mary Reyes Ballista et al.
Frontiers in cell and developmental biology, 11, 1085913-1085913 (2023-02-07)
Chikungunya virus (CHIKV) is the causative agent of the human disease chikungunya fever, characterized by debilitating acute and chronic arthralgia. No licensed vaccines or antivirals are currently available for CHIKV. Therefore, the prevention of attachment of viral particles to host
McLean, M.W., et al.
Proc. 8th Int. Symp. Glycoconjugates, 1, 73-73 (1985)
David Shaya et al.
The Journal of biological chemistry, 285(26), 20051-20061 (2010-04-21)
Heparinase II (HepII) is an 85-kDa dimeric enzyme that depolymerizes both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Recently, we determined the crystal structure of HepII from Pedobacter heparinus (previously known as Flavobacterium heparinum) in complex with a
R F Sewell et al.
The Biochemical journal, 264(3), 777-783 (1989-12-15)
Xyloside-initiated 35SO4(2-)-labelled glycosaminoglycans were isolated from the medium of cultured bovine glomeruli and covalently coupled to Sepharose 4B to construct a solid-phase substrate suitable for the detection of endoglycosidases. The substrate is rendered specific for heparitinase by prior digestion with
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